ID A0A151IZE8_9HYME Unreviewed; 1270 AA.
AC A0A151IZE8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Lysine-specific demethylase 6A {ECO:0000313|EMBL:KYN14441.1};
GN ORFNames=ALC57_13359 {ECO:0000313|EMBL:KYN14441.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN14441.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN14441.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN14441.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN14441.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ980710; KYN14441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151IZE8; -.
DR STRING; 471704.A0A151IZE8; -.
DR Proteomes; UP000078492; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1370; -; 1.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR046941; KDM6_GATAL_sf.
DR InterPro; IPR048562; KDM6A_B-like_C-hel.
DR InterPro; IPR048560; KDM6A_B-like_GATAL.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14017:SF1; LD02225P; 1.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KYN14441.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:KYN14441.1}.
FT REPEAT 28..61
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 219..252
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 942..1105
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 348..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 141120 MW; F3EB3D8F90A53992 CRC64;
MTIFFFLVAA MSAYQKFYSL KGDYWKDASF LYGLGLVYFH FNAFQWAVKA FQQVLWVEPG
FPRACEVHLR LGLMLKVHAE FDAALKHLTL ALIDATTPAS FSKLEIKFHI AHLYEVQGKY
RLAKEHYEAL LKEKLPLHLK ADIYRQLGWM YHVVECTVLG ITRAQKQFTA IHCLQKSIEA
EPKSGQSLYL LGRCLAASGK VHEAFIAYRN SVEKSEGNAD TWCSIGVLYQ QQNQPMDALQ
AYICAVQLDK SHSAAWTNLG ILYESVSQPK DALACYVNAS SNIANCTGPF AGLGGVKSGG
NNPMNPSLQQ RISFLQSHLS QAPMPSVANK RRQLPSIEEA WNLPISAEMS SRQQQQQQQP
GGPSYKYGAT PTGPPPPYPQ AQGQTAKRFK QQLQMLHFLQ QNINSLTPQQ QNVLVQLQHQ
YRAMQQHQQQ IRQQQQAGQR GLRPGQPGYP TAYSHPQNLG QSSGTVALQT GFSDTNVGYN
TAATGNTTQT PGMPYKSASD PTYPPQRQPI TGSAQYGGQY QQQPNQYAAQ GYTQVTSATS
GYSESSTATT ANKDNLGVTD QELQALLSQK DIATSLAEDL LKHFGSDDLE TVVKEEPSSG
VINDNGTLSS GPFSPSNLEE NAADKVKEVK LEKPEEAASQ STQSKSTIDA VTTIMTTTAT
TTVTTVKCET TAVKCETTTS SLSSSTTMTT ATINKNEATN ISKAETMMNL KLELLCESQP
EQELSIEMDA RAVIEACKGR GLKGVPNCSI LSDRSPPPAP PDPPIQRIHL TKEQLSPPAP
SVFLENKKDV FGPQLQEFCL KHPIAVVRGL AAALKLDLGL FSTKTLVEAN PDHGIEVRTQ
MQQTSEENWD PTLNKKVWNC ISHRSHTTIA KYAQYQASSF QESLREEKAQ GGVHVSNLSD
SDSKDSTGQT VRRKKNTFGL AGRPGTKMLR FGTNVDLSDE RKWKPQLHEL MKLPAFARVV
SAGNMLSHVG HVILGMNTVQ LYMKVPGSRT PGHQENNNFC SININIGPGD CEWFAVPDAY
WGVICSLCER NGISYLHGSW WPNLEELFEE NIPVYRFHQR PGDLVWVNAG CVHWVQAVGW
CNNIAWNVGP LTARQYQLAI ERYEWNKLQA FKSIVPMVHL SWNLARNIKV SDPRLFELIK
NCLLRTMRQC CLILEFVKSK NVEVRFHGRG KNEASHYCGQ CEIEVFNILF IREQEKRHVV
HCIDCARKQS PSLEGFVCLE EYRMRDLMDV YDGFTLYTPL VTPTSTTTTT SSSSSSTVST
TLQTQTGQSS
//
